R
Robert Visse
Researcher at Imperial College London
Publications - 26
Citations - 9103
Robert Visse is an academic researcher from Imperial College London. The author has contributed to research in topics: Collagenase & Matrix metalloproteinase. The author has an hindex of 19, co-authored 26 publications receiving 8342 citations. Previous affiliations of Robert Visse include Florida Atlantic University & Arthritis Research UK.
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Journal ArticleDOI
Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry.
Robert Visse,Hideaki Nagase +1 more
TL;DR: This review describes the members of the matrixin family and discusses substrate specificity, domain structure and function, the activation of proMMPs, the regulation of matrixin activity by tissue inhibitors of metalloproteinases, and their pathophysiological implication.
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Structure and function of matrix metalloproteinases and TIMPs
TL;DR: The members of the MMP family are introduced and their domain structure and function, proenyme activation, the mechanism of inhibition by TIMPs and their significance in physiology and pathology are discussed.
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Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis
Linda Chung,Linda Chung,Deendayal Dinakarpandian,Naoto Yoshida,Janelle L. Lauer-Fields,Janelle L. Lauer-Fields,Gregg B. Fields,Gregg B. Fields,Robert Visse,Hideaki Nagase,Hideaki Nagase +10 more
TL;DR: It is reported that collagenases bind and locally unwind the triple‐helical structure before hydrolyzing the peptide bonds and shows that MMP‐1 preferentially interacts with the α2(I) chain of type I collagen and cleaves the three α chains in succession.
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Structural insights into triple-helical collagen cleavage by matrix metalloproteinase 1.
Szymon W. Manka,Federico Carafoli,Robert Visse,Dominique Bihan,Nicolas Raynal,Richard W. Farndale,Gillian Murphy,Jan J. Enghild,Erhard Hohenester,Hideaki Nagase +9 more
TL;DR: Temperature-dependent binding of a catalytically inactive MMP-1 mutant (E200A) to collagen through the cooperative action of its catalytic and hemopexin domains is reported, which may lead to the first transition state of collagenolysis.
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X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding.
Daniela Jozic,Gleb Bourenkov,Ngee Han Lim,Robert Visse,Hideaki Nagase,Wolfram Bode,Klaus Maskos +6 more
TL;DR: This work crystallized recombinant human proMMP-1 and determined its structure to 2.2 Å resolution, providing the first evidence of mobility of the Hpx domain in relation to the catalytic domain, providing an important clue toward the understanding of the collagenase-collagen interaction and subsequent collagenolysis.